Structural consequences of effector protein complex formation in a diiron hydroxylase
Structural consequences of effector protein complex formation in a diiron hydroxylase
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DOI：
10.1073/pnas.0807948105
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发表时间：
2008-12-09
影响因子：
11.1
通讯作者：
Fox, Brian G.
中科院分区：
文献类型：
--
作者：
Bailey, Lucas J.;Mccoy, Jason G.;Fox, Brian G.
羧酸桥二铁羟化酶是多组分酶复合物，负责多种碳氢化合物的分解代谢，因此其作用机制以及在生物修复和酶合成中的潜在用途引起了人们的关注。这些酶复合物使用小分子量效应蛋白来调节羟化酶的功能。然而，人们对这些功能变化的起源知之甚少。在这里，我们报道了两种氧化还原态的甲苯4-单加氧酶的生物学相关效应蛋白-羟化酶复合物的结构。这些结构揭示了许多协调变化，这些变化发生在距离活性位点最远 25 埃的地方，并平衡了催化中心。结果为在与效应蛋白结合相关的许多可测量特性中观察到的变化提供了结构基础。该描述提供了对所有羧酸桥二铁羟化酶中效应蛋白结合的功能作用的深入了解。
Carboxylate-bridged diiron hydroxylases are multicomponent enzyme complexes responsible for the catabolism of a wide range of hydrocarbons and as such have drawn attention for their mechanism of action and potential uses in bioremediation and enzymatic synthesis. These enzyme complexes use a small molecular weight effector protein to modulate the function of the hydroxylase. However, the origin of these functional changes is poorly understood. Here, we report the structures of the biologically relevant effector protein-hydroxylase complex of toluene 4-monooxygenase in 2 redox states. The structures reveal a number of coordinated changes that occur up to 25 angstrom from the active site and poise the diiron center for catalysis. The results provide a structural basis for the changes observed in a number of the measurable properties associated with effector protein binding. This description provides insight into the functional role of effector protein binding in all carboxylate-bridged diiron hydroxylases.